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Updated: Aug 2, 2026

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE
Published on: May 16, 2017
Structure of mouse L-chain ferritin at 1.6 A resolution
T Granier1, B Gallois, B Langlois d'Estaintot
1Unité de Biophysique Structurale, UMR CNRS 5471, Université Bordeaux I, Bâtiment B8, Avenue des Facultés, 33405 Talence CEDEX, France. t.granier@ubs.u-bordeaux.fr
Abstract:
Cubic F432 crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 A resolution from data obtained at room temperature and under cryogenic conditions, respectively. The structure of an eight-amino-acid loop insertion in the mouse sequence is found to be highly disordered both at room temperature and at low temperature.

